1ZS4

Structure of bacteriophage lambda cII protein in complex with DNA

Summary for 1ZS4

• Entry DOI: 10.2210/pdb1zs4/pdb
• Related: 1ZPQ
• Descriptor: DNA - 27mer, Regulatory protein CII, ... (4 entities in total)
• Functional Keywords: helix-turn-helix, transcription activator, transcription-dna complex, transcription/dna
• Biological source: Enterobacteria phage lambda; More
• Total number of polymer chains: 6
• Total formula weight: 53870.30

Authors

Jain, D.,Kim, Y.,Maxwell, K.L.,Beasley, S.,Gussin, G.N.,Edwards, A.M.,Darst, S.A. (deposition date: 2005-05-23, release date: 2005-08-23, Last modification date: 2024-02-14)

Primary citation

Jain, D.,Kim, Y.,Maxwell, K.L.,Beasley, S.,Zhang, R.,Gussin, G.N.,Edwards, A.M.,Darst, S.A.
Crystal Structure of Bacteriophage lambdacII and Its DNA Complex.
Mol.Cell, 19:259-269, 2005

PubMed Abstract: The tetrameric cII protein from bacteriophage lambda activates transcription from the phage promoters P(RE), P(I), and P(AQ) by binding to two direct repeats that flank the promoter -35 element. Here, we present the X-ray crystal structure of cII alone (2.8 A resolution) and in complex with its DNA operator from P(RE) (1.7 A resolution). The structures provide a basis for modeling of the activation complex with the RNA polymerase holoenzyme, and point to the key role for the RNA polymerase alpha subunit C-terminal domain (alphaCTD) in cII-dependent activation, which forms a bridge of protein/protein interactions between cII and the RNA polymerase sigma subunit. The model makes specific predictions for protein/protein interactions between cII and alphaCTD, and between alphaCTD and sigma, which are supported by previous genetic studies.

PubMed: 16039594
DOI: 10.1016/j.molcel.2005.06.006

Experimental method

X-RAY DIFFRACTION (1.7 Å)